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1.A.6.1.1
Epithelial Na+ channel, ENaC (regulates salt and fluid homeostasis and blood pressure; regulated by Nedd4 isoforms and SGK1, 2 and 3 kinases) (Henry et al., 2003; Pao 2012).  Cd2+ inhibits α-ENaC by binding to the internal pore where it interacts with residues in TMS2 (Takeda et al., 2007).  The channel is regulated by palmitoylation of the beta subunit which modulates gating (Mueller et al. 2010). ENaCs are more selective for Naa+ over other cations than ASICs (Yang and Palmer 2018). ENaC plays a role in chronic obstructive pulmonary diseases (COPD) (Zhao et al. 2014). The hetrodimeric complex can consist of αβγ or δβγ subunits, depending on the tissue (Giraldez et al. 2012).  The α- and γ-subunits of the epithelial Na+ channel interact directly with the Na+:Cl- cotransporter, NCC, in the renal distal tubule with functional cosequences, and together they determine bodily salt balance and blood pressure (Mistry et al. 2016).  ENaC is regulated by syntaxins (Saxena et al. 2006). The cryoEM structure has been solved (Noreng et al. 2018). Interactions between the epithelial sodium channel gamma-subunit and claudin-8 modulates paracellular sodium permeability in the renal collecting duct (Sassi et al. 2020).

Accession Number:P51172
Protein Name:Amiloride-sensitive sodium channel subunit delta
Length:638
Molecular Weight:70215.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Na+

Cross database links:

Drugbank: Drugbank Link   

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAEHRSMDGR MEAATRGGSH LQAAAQTPPR PGPPSAPPPP PKEGHQEGLV ELPASFRELL 
61:	TFFCTNATIH GAIRLVCSRG NRLKTTSWGL LSLGALVALC WQLGLLFERH WHRPVLMAVS 
121:	VHSERKLLPL VTLCDGNPRR PSPVLRHLEL LDEFARENID SLYNVNLSKG RAALSATVPR 
181:	HEPPFHLDRE IRLQRLSHSG SRVRVGFRLC NSTGGDCFYR GYTSGVAAVQ DWYHFHYVDI 
241:	LALLPAAWED SHGSQDGHFV LSCSYDGLDC QARQFRTFHH PTYGSCYTVD GVWTAQRPGI 
301:	THGVGLVLRV EQQPHLPLLS TLAGIRVMVH GRNHTPFLGH HSFSVRPGTE ATISIREDEV 
361:	HRLGSPYGHC TAGGEGVEVE LLHNTSYTRQ ACLVSCFQQL MVETCSCGYY LHPLPAGAEY 
421:	CSSARHPAWG HCFYRLYQDL ETHRLPCTSR CPRPCRESAF KLSTGTSRWP SAKSAGWTLA 
481:	TLGEQGLPHQ SHRQRSSLAK INIVYQELNY RSVEEAPVYS VPQLLSAMGS LCSLWFGASV 
541:	LSLLELLELL LDASALTLVL GGRRLRRAWF SWPRASPASG ASSIKPEASQ MPPPAGGTSD 
601:	DPEPSGPHLP RVMLPGVLAG VSAEESWAGP QPLETLDT